Identification and quantitation of signal molecule-dependent protein phosphorylation

Handle URI:
http://hdl.handle.net/10754/562969
Title:
Identification and quantitation of signal molecule-dependent protein phosphorylation
Authors:
Groen, Arnoud J.; Thomas, Ludivine; Lilley, Kathryn S.; Marondedze, Claudius
Abstract:
Phosphoproteomics is a fast-growing field that aims at characterizing phosphorylated proteins in a cell or a tissue at a given time. Phosphorylation of proteins is an important regulatory mechanism in many cellular processes. Gel-free phosphoproteome technique involving enrichment of phosphopeptide coupled with mass spectrometry has proven to be invaluable to detect and characterize phosphorylated proteins. In this chapter, a gel-free quantitative approach involving 15N metabolic labelling in combination with phosphopeptide enrichment by titanium dioxide (TiO2) and their identification by MS is described. This workflow can be used to gain insights into the role of signalling molecules such as cyclic nucleotides on regulatory networks through the identification and quantification of responsive phospho(proteins). © Springer Science+Business Media New York 2013.
KAUST Department:
Biological and Environmental Sciences and Engineering (BESE) Division; Core Labs
Publisher:
Humana Press
Journal:
Methods in Molecular Biology
Issue Date:
3-Sep-2013
DOI:
10.1007/978-1-62703-441-8-9
PubMed ID:
23681576
Type:
Article
ISSN:
10643745
ISBN:
9781627034401
Appears in Collections:
Articles; Biological and Environmental Sciences and Engineering (BESE) Division

Full metadata record

DC FieldValue Language
dc.contributor.authorGroen, Arnoud J.en
dc.contributor.authorThomas, Ludivineen
dc.contributor.authorLilley, Kathryn S.en
dc.contributor.authorMarondedze, Claudiusen
dc.date.accessioned2015-08-03T11:17:26Zen
dc.date.available2015-08-03T11:17:26Zen
dc.date.issued2013-09-03en
dc.identifier.isbn9781627034401en
dc.identifier.issn10643745en
dc.identifier.pmid23681576en
dc.identifier.doi10.1007/978-1-62703-441-8-9en
dc.identifier.urihttp://hdl.handle.net/10754/562969en
dc.description.abstractPhosphoproteomics is a fast-growing field that aims at characterizing phosphorylated proteins in a cell or a tissue at a given time. Phosphorylation of proteins is an important regulatory mechanism in many cellular processes. Gel-free phosphoproteome technique involving enrichment of phosphopeptide coupled with mass spectrometry has proven to be invaluable to detect and characterize phosphorylated proteins. In this chapter, a gel-free quantitative approach involving 15N metabolic labelling in combination with phosphopeptide enrichment by titanium dioxide (TiO2) and their identification by MS is described. This workflow can be used to gain insights into the role of signalling molecules such as cyclic nucleotides on regulatory networks through the identification and quantification of responsive phospho(proteins). © Springer Science+Business Media New York 2013.en
dc.publisherHumana Pressen
dc.subjectGel-free proteomicsen
dc.subjectMass spectrometryen
dc.subjectPhosphoproteomicsen
dc.subjectQuantitationen
dc.subjectTiO2 enrichmenten
dc.titleIdentification and quantitation of signal molecule-dependent protein phosphorylationen
dc.typeArticleen
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Divisionen
dc.contributor.departmentCore Labsen
dc.identifier.journalMethods in Molecular Biologyen
dc.contributor.institutionDepartment of Biochemistry, Cambridge Centre for Proteomics, University of Cambridge, Cambridge, United Kingdomen
kaust.authorThomas, Ludivineen

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